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J. Biol. Chem., Vol. 277, Issue 3, 1637-1640, January 18, 2002
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From the Damaged DNA-binding protein, DDB, is a
heterodimer of p127 and p48 with a high specificity for binding to
several types of DNA damage. Mutations in the p48 gene that
cause the loss of DDB activity were found in a subset of xeroderma
pigmentosum complementation group E (XP-E) patients and have linked to
the deficiency in global genomic repair of cyclobutane pyrimidine
dimers (CPDs) in these cells. Here we show that with a highly defined
system of purified repair factors, DDB can greatly stimulate the
excision reaction reconstituted with XPA, RPA, XPC·HR23B, TFIIH,
XPF·ERCC1 and XPG, up to 17-fold for CPDs and ~2-fold for (6-4)
photoproducts (6-4PPs), indicating that no additional factor is
required for the stimulation by DDB. Transfection of the
p48 cDNA into an SV40-transformed human cell line,
WI38VA13, was found to enhance DDB activity and the in vivo
removal of CPDs and 6-4PPs. Furthermore, the combined technique of
recently developed micropore UV irradiation and immunostaining revealed
that p48 (probably in the form of DDB heterodimer) accumulates at
locally damaged DNA sites immediately after UV irradiation, and this
accumulation is also observed in XP-A and XP-C cells expressing
exogenous p48. These results suggest that DDB can rapidly translocate
to the damaged DNA sites independent of functional XPA and XPC proteins
and directly enhance the excision reaction by core repair factors.
ACCELERATED PUBLICATION
DDB Accumulates at DNA Damage Sites Immediately after UV
Irradiation and Directly Stimulates Nucleotide Excision Repair*
§,,
,,, and§§
Faculty of Pharmaceutical Sciences, Kanazawa
University, Takara-machi, Kanazawa 920-0934, Japan, the
¶ Graduate School of Pharmaceutical Sciences, Hokkaido University,
Kita-ku, Sapporo 060-0812, Japan, the Division of Biochemistry
and Molecular Biology, University of California, Berkeley, California
94720-3202, the ** Department of Biochemistry and Biophysics,
University of North Carolina School of Medicine, Chapel Hill,
North Carolina 27599-7260, and the
Radioisotope Research Center, Nara Medical
University, Kashihara, Nara 634-8521, Japan
*
This work was supported by grants from Ministry of
Education, Culture, Sports, Science and Technology of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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